ID SEPT2_HUMAN Reviewed; 361 AA.
AC Q15019; B4DGE8; Q14132; Q53QU3; Q8IUK9; Q96CB0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 12-APR-2017, entry version 187.
DE RecName: Full=Septin-2;
DE AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 5;
DE Short=NEDD-5;
GN Name=SEPT2; Synonyms=DIFF6, KIAA0158, NEDD5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8697812;
RA Mori T., Miura K., Fujiwara T., Shin S., Inazawa J., Nakamura Y.;
RT "Isolation and mapping of a human gene (DIFF6) homologous to yeast
RT CDC3, CDC10, CDC11, and CDC12, and mouse Diff6.";
RL Cytogenet. Cell Genet. 73:224-227(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hu G.;
RT "Human homolog of mouse Nedd5 mRNA.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 51-66, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP PHOSPHORYLATION AT SER-218.
RX PubMed=15150837; DOI=10.1002/rcm.1453;
RA She Y.M., Huang Y.W., Zhang L., Trimble W.S.;
RT "Septin 2 phosphorylation: theoretical and mass spectrometric evidence
RT for the existence of a single phosphorylation site in vivo.";
RL Rapid Commun. Mass Spectrom. 18:1123-1130(2004).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=15915442; DOI=10.1002/path.1789;
RA Hall P.A., Jung K., Hillan K.J., Russell S.E.H.;
RT "Expression profiling the human septin gene family.";
RL J. Pathol. 206:269-278(2005).
RN [10]
RP INTERACTION WITH MAP4, AND COORDINATED EXPRESSION WITH SEPT2 AND
RP SEPT7.
RX PubMed=16093351; DOI=10.1091/mbc.E05-03-0267;
RA Kremer B.E., Haystead T., Macara I.G.;
RT "Mammalian septins regulate microtubule stability through interaction
RT with the microtubule-binding protein MAP4.";
RL Mol. Biol. Cell 16:4648-4659(2005).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15774761; DOI=10.1126/science.1106823;
RA Spiliotis E.T., Kinoshita M., Nelson W.J.;
RT "A mitotic septin scaffold required for mammalian chromosome
RT congression and segregation.";
RL Science 307:1781-1785(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP INTERACTION WITH SEPT6 AND SEPT7.
RX PubMed=16914550; DOI=10.1074/jbc.M605179200;
RA Low C., Macara I.G.;
RT "Structural analysis of septin 2, 6, and 7 complexes.";
RL J. Biol. Chem. 281:30697-30706(2006).
RN [14]
RP FUNCTION.
RX PubMed=17803907; DOI=10.1016/j.cell.2007.06.053;
RA Kremer B.E., Adang L.A., Macara I.G.;
RT "Septins regulate actin organization and cell-cycle arrest through
RT nuclear accumulation of NCK mediated by SOCS7.";
RL Cell 130:837-850(2007).
RN [15]
RP FUNCTION, AND COLOCALIZATION WITH POLYGLUTAMYLATED TUBULIN.
RX PubMed=18209106; DOI=10.1083/jcb.200710039;
RA Spiliotis E.T., Hunt S.J., Hu Q., Kinoshita M., Nelson W.J.;
RT "Epithelial polarity requires septin coupling of vesicle transport to
RT polyglutamylated microtubules.";
RL J. Cell Biol. 180:295-303(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [22]
RP PHOSPHORYLATION AT SER-218, MUTAGENESIS OF SER-218, AND TISSUE
RP SPECIFICITY.
RX PubMed=19165576; DOI=10.1007/s11010-008-0020-2;
RA Yu W., Ding X., Chen F., Liu M., Shen S., Gu X., Yu L.;
RT "The phosphorylation of SEPT2 on Ser218 by casein kinase 2 is
RT important to hepatoma carcinoma cell proliferation.";
RL Mol. Cell. Biochem. 325:61-67(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [24]
RP INTERACTION WITH SEPT9, AND ROLE IN BACTERIAL INFECTION.
RX PubMed=19145258; DOI=10.1371/journal.pone.0004196;
RA Mostowy S., Nam Tham T., Danckaert A., Guadagnini S.,
RA Boisson-Dupuis S., Pizarro-Cerda J., Cossart P.;
RT "Septins regulate bacterial entry into host cells.";
RL PLoS ONE 4:E4196-E4196(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211 AND SER-218, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [32]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25588830; DOI=10.1242/jcs.158998;
RA Kuo Y.C., Shen Y.R., Chen H.I., Lin Y.H., Wang Y.Y., Chen Y.R.,
RA Wang C.Y., Kuo P.L.;
RT "SEPT12 orchestrates the formation of mammalian sperm annulus by
RT organizing core octomeric complexes with other SEPT proteins.";
RL J. Cell Sci. 128:923-934(2015).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-315 IN COMPLEXES WITH GTP,
RP ELECTRON MICROSCOPY, MUTAGENESIS OF PHE-156; TRP-260 AND HIS-270, AND
RP SUBUNIT.
RX PubMed=17637674; DOI=10.1038/nature06052;
RA Sirajuddin M., Farkasovsky M., Hauer F., Kuehlmann D., Macara I.G.,
RA Weyand M., Stark H., Wittinghofer A.;
RT "Structural insight into filament formation by mammalian septins.";
RL Nature 449:311-315(2007).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-320 IN COMPLEX WITH GDP,
RP AND SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Human septin 2 in complex with GDP.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Forms a
CC filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4
CC at the sperm annulus which is required for the structural
CC integrity and motility of the sperm tail during postmeiotic
CC differentiation (PubMed:25588830). Required for normal
CC organization of the actin cytoskeleton. Plays a role in the
CC biogenesis of polarized columnar-shaped epithelium by maintaining
CC polyglutamylated microtubules, thus facilitating efficient vesicle
CC transport, and by impeding MAP4 binding to tubulin. Required for
CC the progression through mitosis. Forms a scaffold at the midplane
CC of the mitotic splindle required to maintain CENPE localization at
CC kinetochores and consequently chromosome congression. During
CC anaphase, may be required for chromosome segregation and spindle
CC elongation. Plays a role in ciliogenesis and collective cell
CC movements. In cilia, required for the integrity of the diffusion
CC barrier at the base of the primary cilium that prevents diffusion
CC of transmembrane proteins between the cilia and plasma membranes:
CC probably acts by regulating the assembly of the tectonic-like
CC complex (also named B9 complex) by localizing TMEM231 protein. May
CC play a role in the internalization of 2 intracellular microbial
CC pathogens, Listeria monocytogenes and Shigella flexneri.
CC {ECO:0000269|PubMed:15774761, ECO:0000269|PubMed:17803907,
CC ECO:0000269|PubMed:18209106, ECO:0000269|PubMed:19145258,
CC ECO:0000305|PubMed:25588830}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein
CC complexes that form filaments, and associate with cellular
CC membranes, actin filaments and microtubules. GTPase activity is
CC required for filament formation. Filaments are assembled from
CC asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7
CC that associate head-to-head to form a hexameric unit. Interaction
CC between SEPT2 and SEPT7 seems indirect. Interacts with SEPT5 (By
CC similarity). Interaction with SEPT4 not detected (By similarity).
CC Interacts with SEPT9. Component of a septin core octomeric complex
CC consisting of SEPT12, SEPT7, SEPT6 and SEPT2 or SEPT4 in the order
CC 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm
CC annulus. Interacts with MAP4. {ECO:0000250,
CC ECO:0000269|PubMed:16093351, ECO:0000269|PubMed:16914550,
CC ECO:0000269|PubMed:17637674, ECO:0000269|PubMed:19145258,
CC ECO:0000269|PubMed:25588830, ECO:0000269|Ref.35}.
CC -!- INTERACTION:
CC Q9H8W4:PLEKHF2; NbExp=3; IntAct=EBI-741220, EBI-742388;
CC Q8IYM1:SEPT12; NbExp=7; IntAct=EBI-741220, EBI-2585067;
CC Q99719:SEPT5; NbExp=3; IntAct=EBI-741220, EBI-373345;
CC Q14141:SEPT6; NbExp=10; IntAct=EBI-741220, EBI-745901;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15774761}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15774761}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:15774761}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:15774761}. Cleavage
CC furrow {ECO:0000269|PubMed:15774761}. Midbody
CC {ECO:0000269|PubMed:15774761}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:15774761}. Cell projection, cilium membrane
CC {ECO:0000250}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:25588830}. Note=In metaphase cells, localized
CC within the microtubule spindle. At the metaphase plate, in close
CC apposition to the kinetochores of the congressed chromosomes. In
CC cells undergoing cytokinesis, localized to the midbody, the
CC ingressing cleavage furrow, and the central spindle. During
CC bacterial infection, displays a collar shape structure next to
CC actin at the pole of invading bacteria. In epithelial cells,
CC colocalizes with polyglutamylated tubulin around the trans-Golgi
CC network, as well as juxatnuclear and proximal Golgi apparatus.
CC Localizes at the base of the cilia near the morphological
CC distinction between the cilia and plasma membranes. Found in the
CC sperm annulus (PubMed:25588830). {ECO:0000269|PubMed:25588830}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15019-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15019-2; Sequence=VSP_038271;
CC Note=No experimental confirmation available.;
CC Name=3;
CC IsoId=Q15019-3; Sequence=VSP_055176;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Widely expressed. Up-regulated in liver
CC cancer. {ECO:0000269|PubMed:15915442,
CC ECO:0000269|PubMed:19165576}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPT6 and SEPT7.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
CC like GTPase superfamily. Septin GTPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY14718.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA09928.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SEPT2ID44125ch2q37.html";
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DR EMBL; D63878; BAA09928.2; ALT_INIT; mRNA.
DR EMBL; D28540; BAA05893.1; -; mRNA.
DR EMBL; AF038404; AAB92377.1; -; mRNA.
DR EMBL; AK294563; BAG57759.1; -; mRNA.
DR EMBL; AC005104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104841; AAY14718.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC014455; AAH14455.1; -; mRNA.
DR EMBL; BC033559; AAH33559.1; -; mRNA.
DR CCDS; CCDS2548.1; -. [Q15019-1]
DR CCDS; CCDS63195.1; -. [Q15019-3]
DR CCDS; CCDS74682.1; -. [Q15019-2]
DR RefSeq; NP_001008491.1; NM_001008491.2. [Q15019-1]
DR RefSeq; NP_001008492.1; NM_001008492.2. [Q15019-1]
DR RefSeq; NP_001269901.1; NM_001282972.1. [Q15019-2]
DR RefSeq; NP_001269902.1; NM_001282973.1. [Q15019-3]
DR RefSeq; NP_001307958.1; NM_001321029.1.
DR RefSeq; NP_001307959.1; NM_001321030.1. [Q15019-1]
DR RefSeq; NP_001307960.1; NM_001321031.1. [Q15019-1]
DR RefSeq; NP_001307961.1; NM_001321032.1. [Q15019-1]
DR RefSeq; NP_001307962.1; NM_001321033.1. [Q15019-1]
DR RefSeq; NP_001307963.1; NM_001321034.1. [Q15019-1]
DR RefSeq; NP_001307964.1; NM_001321035.1. [Q15019-1]
DR RefSeq; NP_004395.1; NM_004404.4. [Q15019-1]
DR RefSeq; NP_006146.1; NM_006155.2. [Q15019-1]
DR RefSeq; XP_016859694.1; XM_017004205.1. [Q15019-1]
DR RefSeq; XP_016859695.1; XM_017004206.1. [Q15019-1]
DR UniGene; Hs.721234; -.
DR PDB; 2QA5; X-ray; 3.40 A; A/B=1-315.
DR PDB; 2QAG; X-ray; 4.00 A; A=1-361.
DR PDB; 2QNR; X-ray; 2.60 A; A/B=22-320.
DR PDBsum; 2QA5; -.
DR PDBsum; 2QAG; -.
DR PDBsum; 2QNR; -.
DR ProteinModelPortal; Q15019; -.
DR SMR; Q15019; -.
DR BioGrid; 110812; 86.
DR DIP; DIP-38220N; -.
DR IntAct; Q15019; 27.
DR MINT; MINT-1433588; -.
DR STRING; 9606.ENSP00000353157; -.
DR iPTMnet; Q15019; -.
DR PhosphoSitePlus; Q15019; -.
DR SwissPalm; Q15019; -.
DR DMDM; 2500769; -.
DR OGP; Q15019; -.
DR EPD; Q15019; -.
DR MaxQB; Q15019; -.
DR PaxDb; Q15019; -.
DR PeptideAtlas; Q15019; -.
DR PRIDE; Q15019; -.
DR TopDownProteomics; Q15019-1; -. [Q15019-1]
DR DNASU; 4735; -.
DR Ensembl; ENST00000360051; ENSP00000353157; ENSG00000168385. [Q15019-1]
DR Ensembl; ENST00000391971; ENSP00000375832; ENSG00000168385. [Q15019-1]
DR Ensembl; ENST00000391973; ENSP00000375834; ENSG00000168385. [Q15019-1]
DR Ensembl; ENST00000401990; ENSP00000385109; ENSG00000168385. [Q15019-3]
DR Ensembl; ENST00000402092; ENSP00000385172; ENSG00000168385. [Q15019-1]
DR Ensembl; ENST00000616972; ENSP00000479861; ENSG00000168385. [Q15019-2]
DR GeneID; 4735; -.
DR KEGG; hsa:4735; -.
DR UCSC; uc002wbc.5; human. [Q15019-1]
DR CTD; 4735; -.
DR DisGeNET; 4735; -.
DR GeneCards; SEPT2; -.
DR HGNC; HGNC:7729; SEPT2.
DR HPA; CAB017190; -.
DR HPA; HPA018481; -.
DR MIM; 601506; gene.
DR neXtProt; NX_Q15019; -.
DR OpenTargets; ENSG00000168385; -.
DR PharmGKB; PA31535; -.
DR eggNOG; KOG2655; Eukaryota.
DR eggNOG; COG5019; LUCA.
DR GeneTree; ENSGT00870000136374; -.
DR HOGENOM; HOG000233586; -.
DR HOVERGEN; HBG065093; -.
DR InParanoid; Q15019; -.
DR KO; K16942; -.
DR OMA; QFMKAIH; -.
DR OrthoDB; EOG091G07TS; -.
DR PhylomeDB; Q15019; -.
DR TreeFam; TF101079; -.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR SIGNOR; Q15019; -.
DR ChiTaRS; SEPT2; human.
DR EvolutionaryTrace; Q15019; -.
DR GeneWiki; SEPT2; -.
DR GenomeRNAi; 4735; -.
DR PRO; PR:Q15019; -.
DR Proteomes; UP000005640; Chromosome 2.
DR Bgee; ENSG00000168385; -.
DR CleanEx; HS_SEPT2; -.
DR ExpressionAtlas; Q15019; baseline and differential.
DR Genevisible; Q15019; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005930; C:axoneme; IDA:GO_Central.
DR GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000145; C:exocyst; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0097730; C:non-motile cilium; IDA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:GO_Central.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0097227; C:sperm annulus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd01850; CDC_Septin; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR InterPro; IPR008113; Septin2.
DR PANTHER; PTHR18884; PTHR18884; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01740; SEPTIN2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle;
KW Cell division; Cell membrane; Cell projection; Centromere; Chromosome;
KW Complete proteome; Cytoplasm; Cytoskeleton; Differentiation;
KW Direct protein sequencing; GTP-binding; Kinetochore; Membrane;
KW Mitosis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Spermatogenesis.
FT CHAIN 1 361 Septin-2.
FT /FTId=PRO_0000173515.
FT DOMAIN 34 306 Septin-type G.
FT NP_BIND 44 51 GTP.
FT NP_BIND 183 191 GTP.
FT REGION 260 270 Important for dimerization.
FT BINDING 78 78 GTP. {ECO:0000250}.
FT BINDING 104 104 GTP; via amide nitrogen. {ECO:0000250}.
FT BINDING 241 241 GTP; via amide nitrogen and carbonyl
FT oxygen.
FT BINDING 256 256 GTP.
FT SITE 156 156 Important for dimerization.
FT MOD_RES 17 17 Phosphotyrosine.
FT {ECO:0000250|UniProtKB:P42208}.
FT MOD_RES 190 190 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 211 211 Phosphotyrosine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 218 218 Phosphoserine.
FT {ECO:0000244|PubMed:17081983,
FT ECO:0000244|PubMed:18088087,
FT ECO:0000244|PubMed:18220336,
FT ECO:0000244|PubMed:18318008,
FT ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:18691976,
FT ECO:0000244|PubMed:19369195,
FT ECO:0000244|PubMed:19690332,
FT ECO:0000244|PubMed:20068231,
FT ECO:0000244|PubMed:21406692,
FT ECO:0000244|PubMed:23186163,
FT ECO:0000244|PubMed:24275569,
FT ECO:0000269|PubMed:15150837,
FT ECO:0000269|PubMed:19165576}.
FT VAR_SEQ 1 1 M -> MPWISEGRATRPCLRVPSARRGDEGLHQRDEASQKM
FT (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_038271.
FT VAR_SEQ 72 72 A -> AALNTRKTLLW (in isoform 3).
FT {ECO:0000303|PubMed:8590280}.
FT /FTId=VSP_055176.
FT MUTAGEN 156 156 F->D: Loss of dimerization.
FT {ECO:0000269|PubMed:17637674}.
FT MUTAGEN 218 218 S->A: Loss of phosphorylation.
FT {ECO:0000269|PubMed:19165576}.
FT MUTAGEN 260 260 W->A: Loss of dimerization.
FT {ECO:0000269|PubMed:17637674}.
FT MUTAGEN 270 270 H->D: Loss of dimerization.
FT {ECO:0000269|PubMed:17637674}.
FT CONFLICT 69 69 P -> S (in Ref. 6; AAH14455).
FT {ECO:0000305}.
FT CONFLICT 360 361 HV -> TCKVMCTYKKSEKTLSWIKKKTFQMHDPAVCFQSL
FT GGCHPHFNSTCA (in Ref. 2; BAA05893).
FT {ECO:0000305}.
FT HELIX 23 34 {ECO:0000244|PDB:2QA5}.
FT STRAND 38 45 {ECO:0000244|PDB:2QNR}.
FT HELIX 50 58 {ECO:0000244|PDB:2QNR}.
FT HELIX 78 83 {ECO:0000244|PDB:2QNR}.
FT STRAND 85 88 {ECO:0000244|PDB:2QNR}.
FT STRAND 95 102 {ECO:0000244|PDB:2QNR}.
FT HELIX 118 133 {ECO:0000244|PDB:2QNR}.
FT STRAND 148 153 {ECO:0000244|PDB:2QNR}.
FT STRAND 155 159 {ECO:0000244|PDB:2QNR}.
FT HELIX 162 171 {ECO:0000244|PDB:2QNR}.
FT TURN 172 174 {ECO:0000244|PDB:2QNR}.
FT STRAND 177 181 {ECO:0000244|PDB:2QNR}.
FT HELIX 184 186 {ECO:0000244|PDB:2QNR}.
FT HELIX 189 205 {ECO:0000244|PDB:2QNR}.
FT HELIX 225 232 {ECO:0000244|PDB:2QNR}.
FT STRAND 236 238 {ECO:0000244|PDB:2QNR}.
FT STRAND 243 245 {ECO:0000244|PDB:2QA5}.
FT STRAND 254 258 {ECO:0000244|PDB:2QNR}.
FT STRAND 261 264 {ECO:0000244|PDB:2QNR}.
FT TURN 268 270 {ECO:0000244|PDB:2QNR}.
FT HELIX 273 282 {ECO:0000244|PDB:2QNR}.
FT HELIX 284 293 {ECO:0000244|PDB:2QNR}.
FT HELIX 295 305 {ECO:0000244|PDB:2QNR}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 34 306 iprf:G_SEPTIN [T]
FT MYHIT 34 312 ipfam:Septin [T]
SQ SEQUENCE 361 AA; 41487 MW; 12CCBBE30806F92F CRC64;
MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT
DLYPERVIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS
YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV
IAKADTLTLK ERERLKKRIL DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV
GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR
SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DGDGGALGHH
V
//
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